1lf1

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Current revision (07:32, 14 February 2024) (edit) (undo)
 
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<StructureSection load='1lf1' size='340' side='right'caption='[[1lf1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
<StructureSection load='1lf1' size='340' side='right'caption='[[1lf1]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[1lf1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillus_globigii"_migula_1900 "bacillus globigii" migula 1900]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LF1 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[1lf1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LF1 FirstGlance]. <br>
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</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Cellulase Cellulase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.4 3.2.1.4] </span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lf1 OCA], [https://pdbe.org/1lf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lf1 ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lf1 OCA], [https://pdbe.org/1lf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1lf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lf1 ProSAT]</span></td></tr>
</table>
</table>
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== Function ==
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[https://www.uniprot.org/uniprot/Q59232_BACSP Q59232_BACSP]
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lf1 ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1lf1 ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
 
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== Publication Abstract from PubMed ==
 
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The crystal structure of an alkaline Bacillus cellulase catalytic core, from glucoside hydrolase family 5, reveals a novel combination of the catalytic machinery of two classic textbook enzymes. The enzyme has the expected two glutamate residues in close proximity to one another in the active-site that are typical of retaining cellulases. However, the proton donor, glutamate 139 is also unexpectedly a member of a serine-histidine-glutamate catalytic triad, forming a novel combination of catalytic machineries. Structure and sequence analysis of glucoside hydrolase family 5 reveal that the triad is highly conserved, but with variations at the equivalent of the serine position. We speculate that the purpose of this novel catalytic triad is to control the protonation of the acid/base glutamate, facilitating the first step of the catalytic reaction, protonation of the substrate, by the proton donor glutamate. If correct, this will be a novel use for a catalytic triad.
 
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A novel combination of two classic catalytic schemes.,Shaw A, Bott R, Vonrhein C, Bricogne G, Power S, Day AG J Mol Biol. 2002 Jul 5;320(2):303-9. PMID:12079387<ref>PMID:12079387</ref>
 
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
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</div>
 
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<div class="pdbe-citations 1lf1" style="background-color:#fffaf0;"></div>
 
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== References ==
 
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<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacillus globigii migula 1900]]
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[[Category: Bacillus subtilis]]
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[[Category: Cellulase]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Bott, R]]
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[[Category: Bott R]]
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[[Category: Bricogne, G]]
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[[Category: Bricogne G]]
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[[Category: Day, A G]]
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[[Category: Day AG]]
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[[Category: Power, S]]
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[[Category: Power S]]
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[[Category: Shaw, A]]
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[[Category: Shaw A]]
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[[Category: Vonrhein, C]]
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[[Category: Vonrhein C]]
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[[Category: Cellulose degradation]]
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[[Category: Hydrolase]]
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Current revision

Crystal Structure of Cel5 from Alkalophilic Bacillus sp.

PDB ID 1lf1

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